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The low ionic strength reaction of human blood relationship between the binding of serum immuno globulin and complement to red blood cells and surface charge of the cells

, : The low ionic strength reaction of human blood relationship between the binding of serum immuno globulin and complement to red blood cells and surface charge of the cells. British Journal of Haematology 42(3): 403-416

Using the sucrose hemolysis reaction of Hartmann and Jenkins as a basic model, the low ionic strength reaction (LISR) of human blood was studied to determine serum Ig [immunoglobulin] uptake by RBC [red blood cells] with saline elution and 125I-IgG uptake, and complement fixation (CF) to RCB with lysis of PNH [paroxysmal nocturnal hemoglobinuria] cells and C3/C4 antiglobulin hemagglutination (AH) of normal cells. The saline eluates contained IgG and IgM and with traces of IgA. Their pH optima for the uptake by RBC were 6.0 .+-. 0.5, 5.5 .+-. 0.5 and approximately 5.0, respectively. The ratio of bound IgG to IgM was linearly related to the uptake pH. C4 AH and lysis were optimum at pH 6.0-7.5, whereas the maximum C3 AH was at pH 6.0 .+-. 0.5. The LISR performed at a constant pH (6.1 .+-. 0.1) showed that an increasing concentration of neuraminidase (VCN) used in pretreatment of RCB was associated with a decrease in IgG uptake and CF activity. A maximum VCN effect reduced the Ig uptake to approximately 20% of normal and abolished almost all the CF activity. An impaired LISR to various degrees was also observed with RBC pretreated with ficin, papain, bromelin, trypsin or protamine, and RCB from 2 individuals of En(a-) type. Preincubation of serum at LIS with and without RBC resulted in, respectively, a complete and partial consumption of C in the fluid phase. The latter was not enhanced or inhibited by the addition of VCN-treated RBC for preincubation. In the LISR the Ig uptake by RBC is an electrostatic interaction of the oppositely charged RBC and Ig and the CF to RBC results from C activation by the cell-bound IgG and IgM. A pH-dependent inactivation of the cell-bound C3 in the LISR was demonstrated.

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